In order to effectively characterize the gene modulation and transcriptional regulation in eukaryotic cells as well as in various diseases it is necessary to isolate the DNAs and the specific proteins, known as transcription factors (Mitchell and Tjian, 1989; Crabtree and Clipstone, 1994; and Rao et al., 1997), either from tissue samples obtained from different disorders or the cells collected from them grown in culture. The DNAs and proteins isolated from various sources must be intact and undegraded in order to be analyzed by various molecular techniques to evaluate their roles in pathogenic processes. It is often necessary to isolate various DNAs and proteins from a large number of samples over a short time period to determine when a specific gene activation occurs via modulation of a transcription factor, and to utilize them as land marks for identification of different disorders. However, such procedures are generally difficult and cumbersome. Most importantly these proteins should bind to specific DNA sequence motifs (Singh et al., 1985; Sen and Baltimore, 1986a,b; Gilman, et al., 1986; Angel, et al., 1987; Pierce, et al., 1988; Rauscher et al., 1988; Smeal, et al., 1989) and also be recognizable by specific antibodies. Over the past years, various protocols have been developed for the isolation of DNAs as well as the nuclear and cytoplasmic proteins which are involved in transcriptional modulation (Dignam et al., 1983a,b; Kadonaga and Tjian, 1986; Karpen, et al., 1988; Sambrook, et al., 1989; Fiering et al., 1990). However, the majority of these protocols require several steps of purification and high speed centrifugation which involves a significant time lapse between the collection of samples, and substantial physical contact with the laboratory workers. Moreover, the simultaneous isolation of DNAs and transcription factors is rather difficult in a short time span, which is an important aspect, for a sequential evaluation of gene modulation.
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